ID A0A0R2CBZ0_9LACO Unreviewed; 551 AA.
AC A0A0R2CBZ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KRM89326.1};
GN ORFNames=FD21_GL001898 {ECO:0000313|EMBL:KRM89326.1};
OS Liquorilactobacillus vini DSM 20605.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1133569 {ECO:0000313|EMBL:KRM89326.1, ECO:0000313|Proteomes:UP000051576};
RN [1] {ECO:0000313|EMBL:KRM89326.1, ECO:0000313|Proteomes:UP000051576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20605 {ECO:0000313|EMBL:KRM89326.1,
RC ECO:0000313|Proteomes:UP000051576};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM89326.1}.
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DR EMBL; AYYX01000007; KRM89326.1; -; Genomic_DNA.
DR RefSeq; WP_010580416.1; NZ_AYYX01000007.1.
DR AlphaFoldDB; A0A0R2CBZ0; -.
DR STRING; 1133569.FD21_GL001898; -.
DR PATRIC; fig|1133569.4.peg.2053; -.
DR eggNOG; COG0492; Bacteria.
DR eggNOG; COG3634; Bacteria.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000051576; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd03026; AhpF_NTD_C; 1.
DR CDD; cd02974; AhpF_NTD_N; 1.
DR Gene3D; 3.40.30.80; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR044141; AhpF_NTD_C.
DR InterPro; IPR044142; AhpF_NTD_N.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF13192; Thioredoxin_3; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051576}.
FT DOMAIN 7..299
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 473..544
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
SQ SEQUENCE 551 AA; 60053 MW; 32A8E9041F218857 CRC64;
MTEKRIYDTV IIGAGPAGLT AAIYAGRATL DTLVIEADQI GGQVTTTSVV WNYPGVEKVD
GTALMNKMQQ QAAHFGVQLT KDRIAGYDLK DDLKVLHGSK QNYYARSVIL AGGAKPRELD
FPGEKQFRGH GIAFCSTCDG ELFSGLEVFV IGGGYAAAEE ADYLTRYAKH VTVIAREDHF
TCAPLTAARA LNNPKVTVKF NTEIVRVTGQ DYLQTAVFKN NQTGEEFTYQ ADQQAQTFGI
FIYIGTQPAT TGLTGILEHD QHGYLKVDQQ LQTNLPGVFA AGDIVAKPLR QIVTAAGDGA
LAATSAEHYV TALKERLHIP IKRQEKQPAK TVGQTSQLAD DSAASVVHQG AWFPVKMKEQ
LQQILARLTK KVILQVWDDG SQKSQELQSF ATEFCQLDQH LQFQVAPAPS QETYLPVLRL
LNDQQKDTGI RFGGIPTGHE LNSLVLAVYN LAGPGQELSP QLIARIKALP PTRIKIGVAL
TCHFCPDVVA ACQHMAALNP NVSAEMLDLQ LFPELRKQKH IMSVPATMIN DGEVIFGSQT
PEQLVAACEK Q
//